Butterworth, R. F. Hepatic encephalopathy. Alcohol Res. Health 27, 240-246 (2003).
DuBose, T. D. Jr, Good, D. W., Hamm, L. L. & Wall, S. M. Ammonium transport in the kidney: new physiological concepts and their clinical implications. J. Am. Soc. Nephrol. 1, 1193-1203 (1991).
Hamm, L. L. & Simon, E. E. Roles and mechanisms of urinary buffer excretion. Am. J. Physiol. 253, F595-F605 (1987).
Knepper, M. A. NH4+ transport in the kidney. Kidney Int., Suppl. 33, S95-S102 (1991).
Weiner, I. D. & Hamm, L. L. Molecular mechanisms of renal ammonia transport. Annu. Rev. Physiol. 69, 317-340 (2007).
Pitts, R. F. The renal excretion of acid. Fed. Proc. 7, 418-426 (1948).
Sartorius, O. W., Roemmelt, J. C., Pitts, R. F., Calhoon, D. & Miner, P. The renal regulation of acid-base balance in man. IV. The nature of the renal compensations in ammonium chloride acidosis. J. Clin. Invest. 28, 423-439 (1949).
Rodriguez Soriano, J. Renal tubular acidosis: the clinical entity. J. Am. Soc. Nephrol. 13, 2160-2170 (2002).
Laing, C. M., Toye, A. M., Capasso, G. & Unwin, R. J. Renal tubular acidosis: developments in our understanding of the molecular basis. Int. J. Biochem. Cell Biol. 37, 1151-1161 (2005).
Marini, A. M., Vissers, S., Urrestarazu, A. & Andre, B. Cloning and expression of the MEP1 gene encoding an ammonium transporter in Saccharomyces cerevisiae. EMBO J. 13, 3456-3463 (1994).
Ninnemann, O., Jauniaux, J. C. & Frommer, W. B. Identification of a high affinity NH4+ transporter from plants. EMBO J. 13, 3464-3471 (1994).
Marini, A. M., Urrestarazu, A., Beauwens, R. & Andre, B. The Rh (rhesus) blood group polypeptides are related to NH4+ transporters. Trends Biochem. Sci. 22, 460-461 (1997).
Levine, P. & Stetson, R. E. An unusual case of intra-group agglutination. J. Am. Med. Assoc. 113, 126-127 (1939).
Le van Kim, C. et al. Molecular cloning and primary structure of the human blood group RhD polypeptide. Proc. Natl Acad. Sci. USA 89, 10925-10929 (1992).
Cherif-Zahar, B. et al. Organization of the gene (RHCE) encoding the human blood group RhCcEe antigens and characterization of the promoter region. Genomics 19, 68-74 (1994).
Ridgwell, K. et al. Isolation of cDNA clones for a 50 kDa glycoprotein of the human erythrocyte membrane associated with Rh (rhesus) blood-group antigen expression. Biochem. J. 287, 223-228 (1992).
Marini, A. M. et al. The human Rhesus-associated RhAG protein and a kidney homologue promote ammonium transport in yeast. Nature Genet. 26, 341-344 (2000).
Liu, Z. et al. Characterization of human RhCG and mouse Rhcg as novel nonerythroid Rh glycoprotein homologues predominantly expressed in kidney and testis. J. Biol. Chem. 275, 25641-25651 (2000).
Liu, Z., Peng, J., Mo, R., Hui, C. & Huang, C. H. Rh type B glycoprotein is a new member of the Rh superfamily and a putative ammonia transporter in mammals. J. Biol. Chem. 276, 1424-1433 (2001).
Quentin, F. et al. RhBG and RhCG, the putative ammonia transporters, are expressed in the same cells in the distal nephron. J. Am. Soc. Nephrol. 14, 545-554 (2003).
Verlander, J. W. et al. Localization of the ammonium transporter proteins RhBG and RhCG in mouse kidney. Am. J. Physiol. Renal Physiol. 284, F323-F337 (2003).
Eladari, D. et al. Expression of RhCG, a new putative NH 3/NH4+ transporter, along the rat nephron. J. Am. Soc. Nephrol. 13, 1999-2008 (2002).
Bakouh, N. et al. NH3 is involved in the NH 4+ transport induced by the functional expression of the human Rh C glycoprotein. J. Biol. Chem. 279, 15975-15983 (2004).
Benjelloun, F. et al. Expression of the human erythroid Rh glycoprotein (RhAG) enhances both NH3 and NH4+ transport in HeLa cells. Pflugers Arch. 450, 155-167 (2005).
Nakhoul, N. L. et al. Characteristics of renal Rhbg as an NH 4+ transporter. Am. J. Physiol. Renal Physiol. 288, F170-F181 (2005).
Zidi-Yahiaoui, N. et al. Human Rhesus B and Rhesus C glycoproteins: properties of facilitated ammonium transport in recombinant kidney cells. Biochem. J. 391, 33-40 (2005).
Mak, D. O., Dang, B., Weiner, I. D., Foskett, J. K. & Westhoff, C. M. Characterization of ammonia transport by the kidney Rh glycoproteins RhBG and RhCG. Am. J. Physiol. Renal Physiol. 290, F297-F305 (2006).
Mayer, M. et al. Different transport mechanisms in plant and human AMT/Rh-type ammonium transporters. J. Gen. Physiol. 127, 133-144 (2006).
Westhoff, C. M., Ferreri-Jacobia, M., Mak, D. O. & Foskett, J. K. Identification of the erythrocyte Rh blood group glycoprotein as a mammalian ammonium transporter. J. Biol. Chem. 277, 12499-12502 (2002).
Chambrey, R. et al. Genetic ablation of Rhbg in the mouse does not impair renal ammonium excretion. Am. J. Physiol. Renal Physiol. 289, F1281-F1290 (2005).
Endeward, V., Cartron, J. P., Ripoche, P. & Gros, G. RhAG protein of the Rhesus complex is a CO2 channel in the human red cell membrane. FASEB J. 22, 64-73 (2008).
Soupene, E., Inwood, W. & Kustu, S. Lack of the Rhesus protein Rh1 impairs growth of the green alga Chlamydomonas reinhardtii at high CO2. Proc. Natl Acad. Sci. USA 101, 7787-7792 (2004).
Ji, Q. et al. CeRh1 (rhr-1) is a dominant Rhesus gene essential for embryonic development and hypodermal function in Caenorhabditis elegans. Proc. Natl Acad. Sci. USA 103, 5881-5886 (2006).
Missner, A. et al. Carbon dioxide transport through membranes. J. Biol. Chem. 283, 25340-25347 (2008).
May, R. C., Kelly, R. A. & Mitch, W. E. Metabolic acidosis stimulates protein degradation in rat muscle by a glucocorticoid-dependent mechanism. J. Clin. Invest. 77, 614-621 (1986).
Bevensee, M. O. & Boron, W. F. Control of Intracellular pH (eds Alpern, R. J. & Hebert, S. C.) 1429-1490 (Elsevier Inc., 2008).
Pastor-Soler, N., Pietrement, C. & Breton, S. Role of acid/base transporters in the male reproductive tract and potential consequences of their malfunction. Physiology (Bethesda) 20, 417-428 (2005).
Karet, F. E. Inherited distal renal tubular acidosis. J. Am. Soc. Nephrol. 13, 2178-2184 (2002).
Kim, S. C. & Kim, H. W. Effects of nitrogenous components of urine on sperm motility: an in vitro study. Int. J. Androl. 21, 29-33 (1998).
van Straaten, H. W. et al. Cellular concentrations of glutamine synthetase in murine organs. Biochem. Cell Biol. 84, 215-231 (2006).
